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Conserved domains on  [gi|1721675436|gb|QEC74699|]
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HAD-IIA family hydrolase [Mucilaginibacter ginsenosidivorax]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11428959)

haloacid dehalogenase (HAD)-IIA family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-254 5.20e-103

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


:

Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 300.10  E-value: 5.20e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:COG0647    10 AFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERHP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMV-DKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAAT 166
Cdd:COG0647    90 GARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAGAL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 167 AAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHL 246
Cdd:COG0647   170 AAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPDY 249


                  ....*...
gi 1721675436 247 VVDSVDEI 254
Cdd:COG0647   250 VLDSLAEL 257
 
Name Accession Description Interval E-value
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-254 5.20e-103

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 300.10  E-value: 5.20e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:COG0647    10 AFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERHP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMV-DKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAAT 166
Cdd:COG0647    90 GARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAGAL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 167 AAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHL 246
Cdd:COG0647   170 AAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPDY 249


                  ....*...
gi 1721675436 247 VVDSVDEI 254
Cdd:COG0647   250 VLDSLAEL 257
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 7-253 1.72e-96

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 282.94  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   7 HGLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHY 86
Cdd:cd07530     1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  87 PGCCVHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPS-PRREGwnnL--GI 163
Cdd:cd07530    81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTlPTERG---LlpGN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 164 AATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYR 243
Cdd:cd07530   158 GSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYR 237

                         250
                  ....*....|
gi 1721675436 244 PHLVVDSVDE 253
Cdd:cd07530   238 PTYIVPSLRE 247
PRK10444 PRK10444
HAD-IIA family hydrolase;
12-255 3.24e-60

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 190.77  E-value: 3.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLtEHYPGCCV 91
Cdd:PRK10444    7 DIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFL-RRQEGKKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  92 HVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDP-----SPrregwnnlGIAAT 166
Cdd:PRK10444   86 YVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDThgrgfYP--------ACGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 167 AAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHL 246
Cdd:PRK10444  158 CAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSW 237


                  ....*....
gi 1721675436 247 VVDSVDEIE 255
Cdd:PRK10444  238 IYPSVADID 246
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 8-253 3.62e-54

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 175.43  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:TIGR01457   3 GYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAATA 167
Cdd:TIGR01457  83 DASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAIPTERGLLPGNGSLT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 168 AMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHLV 247
Cdd:TIGR01457 163 SVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPTHA 242


                  ....*.
gi 1721675436 248 VDSVDE 253
Cdd:TIGR01457 243 IDSLAE 248
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 9-108 4.14e-34

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 118.72  E-value: 4.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   9 LMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYPG 88
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|
gi 1721675436  89 CCVHVLGEGGLLKSLKNAGI 108
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGF 100
 
Name Accession Description Interval E-value
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
8-254 5.20e-103

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 300.10  E-value: 5.20e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:COG0647    10 AFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLAERHP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMV-DKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAAT 166
Cdd:COG0647    90 GARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRTVPTEDGLIPGAGAL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 167 AAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHL 246
Cdd:COG0647   170 AAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPIRPDY 249


                  ....*...
gi 1721675436 247 VVDSVDEI 254
Cdd:COG0647   250 VLDSLAEL 257
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 7-253 1.72e-96

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 282.94  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   7 HGLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHY 86
Cdd:cd07530     1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  87 PGCCVHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPS-PRREGwnnL--GI 163
Cdd:cd07530    81 PGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTlPTERG---LlpGN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 164 AATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYR 243
Cdd:cd07530   158 GSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYR 237

                         250
                  ....*....|
gi 1721675436 244 PHLVVDSVDE 253
Cdd:cd07530   238 PTYIVPSLRE 247
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 8-254 1.17e-65

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 204.73  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:cd07531     2 GYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMVDKKPD--LVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAA 165
Cdd:cd07531    82 NAKVFVTGEEGLIEELRLAGLEIVDKYDEaeYVVVGSNRKITYELLTKAFRACLRGARYIATNPDRIFPAEDGPIPDTAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 166 TAAMIEEATGREP-FVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRP 244
Cdd:cd07531   162 IIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHGYKP 241

                         250
                  ....*....|
gi 1721675436 245 HLVVDSVDEI 254
Cdd:cd07531   242 DYVLNSIKDL 251
PRK10444 PRK10444
HAD-IIA family hydrolase;
12-255 3.24e-60

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 190.77  E-value: 3.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLtEHYPGCCV 91
Cdd:PRK10444    7 DIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFL-RRQEGKKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  92 HVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDP-----SPrregwnnlGIAAT 166
Cdd:PRK10444   86 YVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDThgrgfYP--------ACGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 167 AAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHL 246
Cdd:PRK10444  158 CAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSW 237


                  ....*....
gi 1721675436 247 VVDSVDEIE 255
Cdd:PRK10444  238 IYPSVADID 246
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 8-253 1.94e-59

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 189.50  E-value: 1.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:cd07508     1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMV-------------------DKKPDLVILGEGQEFSLERVHNAVDMILA-GARFIAT 147
Cdd:cd07508    81 GKKVYVLGEEGLKEELRAAGFRIAggpskgietyaelvehledDENVDAVIVGSDFKLNFAKLRKACRYLRNpGCLFIAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 148 NRDPS-PRREGWNNLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTIL 226
Cdd:cd07508   161 APDRIhPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 1721675436 227 VLSGIADKE---QLIKYGYRPHLVVDSVDE 253
Cdd:cd07508   241 VLTGVTTLEdlqAYIDHELVPDYYADSLAD 270
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 10-253 1.21e-55

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized subfamily belongs to the UmpH/NagD phosphatase family and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 179.17  E-value: 1.21e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  10 MIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYPGC 89
Cdd:cd16422     3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  90 CVHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRD---PSPRregwnnlG---- 162
Cdd:cd16422    83 KIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIATHPDincPSEE-------Gpipd 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 163 IAATAAMIEEATGR-EPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYG 241
Cdd:cd16422   156 AGSIIALIETSTGRrPDLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLE 235

                         250
                  ....*....|..
gi 1721675436 242 YRPHLVVDSVDE 253
Cdd:cd16422   236 RKPTYVFDNVGE 247
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 8-253 3.62e-54

HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 175.43  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:TIGR01457   3 GYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCCVHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAATA 167
Cdd:TIGR01457  83 DASVYVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAIPTERGLLPGNGSLT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 168 AMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHLV 247
Cdd:TIGR01457 163 SVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPTHA 242


                  ....*.
gi 1721675436 248 VDSVDE 253
Cdd:TIGR01457 243 IDSLAE 248
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 12-230 7.30e-49

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 161.34  E-value: 7.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKL-AKLGINVTEKHIYTSAMATATFLTEHYPGCC 90
Cdd:TIGR01460   4 DIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLsSLLGVDVSPDQIITSGSVTKDLLRQRFEGEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  91 VHVLGEGGLLKSLKNAGIPMV----------DKKPDLVILGEGQEFSLERVHNAVDMILAG-ARFIATNRDPSPR-REGW 158
Cdd:TIGR01460  84 VYVIGVGELRESLEGLGFRNDffddidhlaiEKIPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDLVRlGDGR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721675436 159 NNLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTI-IGDTMETDIIGGIYMGFKTILVLSG 230
Cdd:TIGR01460 164 FRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFDTLLVLTG 236
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 8-251 2.50e-45

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 153.48  E-value: 2.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLteHYP 87
Cdd:TIGR01452   4 GFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLL--RQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCC---VHVLGEGGLLKSLKNAGIPMV----DKKPDL----------------VILGEGQEFSLERVHNAVDMIL-AGAR 143
Cdd:TIGR01452  82 PDAgkaVYVIGEEGLRAELDAAGIRLAgdpgEKKQDEadgfmydikldervgaVVVGYDEHFSYVKLMEACAHLRePGCL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 144 FIATNRDP-SPRREGWNNLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGF 222
Cdd:TIGR01452 162 FVATNRDPwHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCGM 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1721675436 223 KTILVLSGIADKEQLIKY------GYRPHLVVDSV 251
Cdd:TIGR01452 242 TTVLVLSGVSQLEEAQEYlmagqdDLVPDYVVESL 276
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 8-254 4.24e-45

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 152.93  E-value: 4.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINV-TEKHIYTSAMATATFLTEHY 86
Cdd:cd07510     3 TFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGlKEEEIFSSAYCAARYLRQRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  87 PGCC---VHVLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMILAG---------------------A 142
Cdd:cd07510    83 PGPAdgkVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVGldehvnylklakatqylrdpgC 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 143 RFIATNRDPS-PRREGWNNLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMG 221
Cdd:cd07510   163 LFVATNRDPWhPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCG 242

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1721675436 222 FKTILVLSGIADKEQLIKY---GYRPHLVVDSVDEI 254
Cdd:cd07510   243 LKTLLVLTGVSTLEEALAKlsnDLVPDYYVESLADL 278
PLN02645 PLN02645
phosphoglycolate phosphatase
 12-237 1.30e-44

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 152.56  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFL-TEHYP-GC 89
Cdd:PLN02645   34 DCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLkSINFPkDK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  90 CVHVLGEGGLLKSLKNAGIPMV------DKKPDL--------------VILGEGQEFSLERVHNAVDMIL--AGARFIAT 147
Cdd:PLN02645  114 KVYVIGEEGILEELELAGFQYLggpedgDKKIELkpgflmehdkdvgaVVVGFDRYINYYKIQYATLCIRenPGCLFIAT 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 148 NRDP----SPRREgWNnlGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFK 223
Cdd:PLN02645  194 NRDAvthlTDAQE-WA--GAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCK 270

                         250
                  ....*....|....
gi 1721675436 224 TILVLSGIADKEQL 237
Cdd:PLN02645  271 TLLVLSGVTSESML 284
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 8-251 2.37e-38

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 134.33  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYP 87
Cdd:cd07509     2 AVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  88 GCcvHVLGEGGLLKSLKNagipmVDKK-PDLVILGE-GQEFSLERVHNAVDMILAGARFIATNRDPSPRREGWNNLGIAA 165
Cdd:cd07509    82 RP--HLLVDDDALEDFIG-----IDTSdPNAVVIGDaGEHFNYQTLNRAFRLLLDGAPLIALHKGRYYKRKDGLALDPGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 166 TAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPH 245
Cdd:cd07509   155 FVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTGKYRPSDEKKPNVPPD 234


                  ....*.
gi 1721675436 246 LVVDSV 251
Cdd:cd07509   235 LTADSF 240
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 12-241 5.61e-37

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 132.04  E-value: 5.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIK-AADVFIKRLLKDKIPFtFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYPGCC 90
Cdd:cd07532    12 DADGVLWTGDKPIPgAVEVFNALLDKGKKVF-IVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLKEKGFKKK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  91 VHVLGEGGLLKSLKNAGI---------------------PMVDKKPDLVILGEGQEFSLERVHNAVDMIL-AGARFIATN 148
Cdd:cd07532    91 VYVIGEEGIRKELEEAGIvscggdgedekddsmgdfahnLELDPDVGAVVVGRDEHFSYPKLMKACNYLRnPDVLFLATN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 149 RD---PSPrrEGWNNLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTI 225
Cdd:cd07532   171 MDatfPGP--VGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFANNCGFQSL 248

                         250
                  ....*....|....*....
gi 1721675436 226 LVLSG---IADKEQLIKYG 241
Cdd:cd07532   249 LVGTGvnsLEDAEKIKKEG 267
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 9-108 4.14e-34

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 118.72  E-value: 4.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   9 LMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFLTEHYPG 88
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|
gi 1721675436  89 CCVHVLGEGGLLKSLKNAGI 108
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGF 100
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 8-253 2.85e-27

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 105.71  E-value: 2.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIY-----AGEELIKAADVfIKRLLKDKIPFTFLSNNSSKSRADAVEKLAKLGINVTEKHIYTSAMATATFL 82
Cdd:TIGR01458   3 GVLLDISGVLYisdagGGTAVPGSQEA-VKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  83 TEHypGCCVHVLGEGGLLKSLKnaGIPMVDkkPDLVILGEGQE-FSLERVHNAVDMILAGAR--FIATNRDPSPRREGWN 159
Cdd:TIGR01458  82 EEK--QLRPMLLVDDRVLPDFD--GIDTSD--PNCVVMGLAPEhFSYQILNQAFRLLLDGAKpvLIAIGKGRYYKRKDGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 160 NLGIAATAAMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIK 239
Cdd:TIGR01458 156 ALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEEK 235

                         250
                  ....*....|....
gi 1721675436 240 YGYRPHLVVDSVDE 253
Cdd:TIGR01458 236 INVPPDLTCDSLPH 249
Hydrolase_like pfam13242
HAD-hyrolase-like;
180-253 1.10e-24

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 93.45  E-value: 1.10e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721675436 180 VIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKYGYRPHLVVDSVDE 253
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAE 74
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 9-249 2.38e-14

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 70.43  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   9 LMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNnSSKSRADAVEKLAKLGIN-VTEKHIYTSAMATATFL--TEH 85
Cdd:cd07525     3 FLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTN-APRPAESVVRQLAKLGVPpSTYDAIITSGEVTRELLarEAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  86 YPGCCVHVLGEG--GLLKSLKNAGIPMVDKKPDLVILGEGqEFSLERVHNAVDMILAGAR----FIATNRDPSPRREGWN 159
Cdd:cd07525    82 LGRKVYHLGPERdaNVLEGLDVVATDDAEKAEFILCTGLY-DDETETPEDYRKLLKAAAArglpLICANPDLVVPRGGKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 160 NLGIAATAAMIEEATGREPFvIGKPSPVMMRSAAAYMG-LQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIA---DKE 235
Cdd:cd07525   161 IYCAGALAELYEELGGEVIY-FGKPHPPIYDLALARLGrPAKARILAVGDGLHTDILGANAAGLDSLFVTGGIHrrlAAE 239

                         250
                  ....*....|....
gi 1721675436 236 QLIKYGYRPHLVVD 249
Cdd:cd07525   240 AGIKSQIVPDFVIP 253
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
12-254 2.56e-13

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 66.88  E-value: 2.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGV-IYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKLakLGINVTE---------KHIYTSAMATATF 81
Cdd:COG0546     7 DLDGTlVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRL--LGEDPDEeleellarfRELYEEELLDETR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  82 LtehYPGccVHvlgegGLLKSLKNAGIPMVdkkpdlvilgegqefslervhnavdmilagarfIATNRDPSPRREGWNNL 161
Cdd:COG0546    85 L---FPG--VR-----ELLEALKARGIKLA---------------------------------VVTNKPREFAERLLEAL 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 162 GIAAtaaMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILVLSGIADKEQLIKYG 241
Cdd:COG0546   122 GLDD---YFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTWGYGSAEELEAAG 197

                         250
                  ....*....|...
gi 1721675436 242 yrPHLVVDSVDEI 254
Cdd:COG0546   198 --ADYVIDSLAEL 208
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
178-235 3.96e-10

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 57.06  E-value: 3.96e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 178 PFVI--GKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSgIADKE 235
Cdd:COG2179    84 PYIAraKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKP-LVDKE 142
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 8-229 1.27e-09

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 57.21  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVeKLAKLGINVTE-KHIYTSA-MATATFLT-- 83
Cdd:TIGR01459  10 VFLLDLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIFSLHK-TLKSLGINADLpEMIISSGeIAVQMILEsk 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  84 ---EHYPGCCVHVlgeGGLLKSLKN-AGIPMV---DKKPDLVILG---EGQEFSLervhNAVDMILA--GAR---FIATN 148
Cdd:TIGR01459  89 krfDIRNGIIYLL---GHLENDIINlMQCYTTddeNKANASLITIyrsENEKLDL----DEFDELFApiVARkipNICAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 149 RDPSPRREGWNNLGIAATAAMIEEATGREPFViGKPSPVMMRSAAAYMGLQPE-QVTIIGDTMETDIIGGIYMGFKTILV 227
Cdd:TIGR01459 162 PDRGINQHGIYRYGAGYYAELIKQLGGKVIYS-GKPYPAIFHKALKECSNIPKnRMLMVGDSFYTDILGANRLGIDTALV 240


                  ..
gi 1721675436 228 LS 229
Cdd:TIGR01459 241 LT 242
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 183-254 1.59e-08

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 53.49  E-value: 1.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILvlsgIADKEQLIKYGYRPHLVVDSVDEI 254
Cdd:COG1011   149 KPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVW----VNRSGEPAPAEPRPDYVISDLAEL 216
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 159-239 2.34e-08

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 52.41  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 159 NNLGiAATAAMIEEATGRePFVIG--KPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQ 236
Cdd:TIGR01668  67 NNAG-EQRAKAVEKALGI-PVLPHavKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQW 144


                  ...
gi 1721675436 237 LIK 239
Cdd:TIGR01668 145 FIK 147
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 178-227 4.21e-08

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 50.34  E-value: 4.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1721675436 178 PFVI--GKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTILV 227
Cdd:cd16416    57 PFVAraGKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 170-225 1.76e-06

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 45.61  E-value: 1.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1721675436 170 IEEATGrepfvIGKPSPVMMRSAAAYMGLQPEQVTIIGDTMETDIIGGIYMGFKTI 225
Cdd:cd04305    56 ISEEVG-----VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 183-254 3.26e-06

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 46.24  E-value: 3.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILVLSGIADKEQLikyGYRPHLVVDSVDEI 254
Cdd:COG0241   102 KPKPGMLLQAAERLGIDLSNSYMIGDR-LSDLQAAKAAGCKGILVLTGKGAEELA---EALPDTVADDLAEA 169
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
12-254 1.28e-05

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 44.81  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  12 DMDGVIYAGEELIKAADvfiKRLLKDK-IPFT--FLSNNSSKSRADAVEKL-AKLGINVTEKHIYT--SAMATATFLTEH 85
Cdd:COG0637     8 DMDGTLVDSEPLHARAW---REAFAELgIDLTeeEYRRLMGRSREDILRYLlEEYGLDLPEEELAArkEELYRELLAEEG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  86 ---YPGccVHvlgegGLLKSLKNAGIPMVdkkpdlvilgegqefslervhnavdmilagarfIATNrdpSPRRegwnnlg 162
Cdd:COG0637    85 lplIPG--VV-----ELLEALKEAGIKIA---------------------------------VATS---SPRE------- 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 163 iaaTAAMIEEATGREPF--VI--------GKPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILVLSGIA 232
Cdd:COG0637   115 ---NAEAVLEAAGLLDYfdVIvtgddvarGKPDPDIYLLAAERLGVDPEECVVFEDS-PAGIRAAKAAGMRVVGVPDGGT 190

                         250       260
                  ....*....|....*....|..
gi 1721675436 233 DKEQLIKygyrPHLVVDSVDEI 254
Cdd:COG0637   191 AEEELAG----ADLVVDDLAEL 208
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 8-88 1.34e-05

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319814  Cd Length: 136  Bit Score: 43.92  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKDKIPFTFLSNNSSKSRADAVEKL-AKLGINVTEKHIYTSamatatflteHY 86
Cdd:cd07511     2 GFAFDIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLsKLLGVEVSPDQVIQS----------HS 71


                  ..
gi 1721675436  87 PG 88
Cdd:cd07511    72 PG 73
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 11-221 1.42e-05

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 44.50  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  11 IDMDGVIYAGEELIkaADVFIKRLLKDKIPFTFlsnnssksradaVEKLAKLGINVTEkHIYTSAMATATFLTEHypgcc 90
Cdd:pfam00702   6 FDLDGTLTDGEPVV--TEAIAELASEHPLAKAI------------VAAAEDLPIPVED-FTARLLLGKRDWLEEL----- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436  91 vhvLGEGGLLKSLKNAGIPMVDKKPDLVILGEGQEFSLERVHNAVDMI-LAGAR-FIATNRDPSPRREGWNNLGIAATAA 168
Cdd:pfam00702  66 ---DILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALkERGIKvAILTGDNPEAAEALLRLLGLDDYFD 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1721675436 169 MIeeaTGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMG 221
Cdd:pfam00702 143 VV---ISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDG-VNDIPAAKAAG 191
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 183-254 1.41e-04

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 41.88  E-value: 1.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILVLSGIADKEQLIKYGyrPHLVVDSVDEI 254
Cdd:cd02616   136 KPDPEPVLKALELLGAEPEEALMVGDS-PHDILAGKNAGVKTVGVTWGYKGREYLKAFN--PDFIIDKMSDL 204
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
183-254 1.63e-04

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 41.72  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILVlsgiadkeqliKYGYR---------PHLVVDSVDE 253
Cdd:PRK13222  149 KPDPAPLLLACEKLGLDPEEMLFVGDS-RNDIQAARAAGCPSVGV-----------TYGYNygepialsePDVVIDHFAE 216


                  .
gi 1721675436 254 I 254
Cdd:PRK13222  217 L 217
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 197-255 1.76e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 41.42  E-value: 1.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1721675436 197 GLQPEQVTIIGDTmETDIIGGIYMGFKTILVLSGIADKEQLIKYGyrPHLVVDSVDEIE 255
Cdd:cd04302   151 GIAPEQAVMIGDR-KHDIIGARANGIDSIGVLYGYGSEDELEEAG--ATYIVETPAELL 206
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 8-74 3.40e-04

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 41.40  E-value: 3.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721675436   8 GLMIDMDGVIYAGEELIKAADVFIKRLLKD----KIPFTFLSNNSSKS-RADAVEKLAKLGINVTEKHIYTS 74
Cdd:TIGR01456   2 GFAFDIDGVLFRGKKPIAGASDALRRLNRNqgqlKIPYIFLTNGGGFSeRARAEEISSLLGVDVSPLQVIQS 73
PRK06769 PRK06769
HAD-IIIA family hydrolase;
183-240 8.24e-04

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 39.33  E-value: 8.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTMeTDIIGGIYMGFKTILVLSGiADKEQLIKY 240
Cdd:PRK06769   93 KPSTGMLLQAAEKHGLDLTQCAVIGDRW-TDIVAAAKVNATTILVRTG-AGYDALHTY 148
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 183-227 8.81e-04

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 38.67  E-value: 8.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFKTILV 227
Cdd:cd07503    99 KPKPGMLLDAAKELGIDLARSFVIGDR-LSDIQAARNAGCKGILV 142
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
144-227 8.84e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 39.10  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 144 FIATNRDPSPRREGWNNLGIAAtaaMIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFK 223
Cdd:pfam13419  99 GIVTSKSRENVEEFLKQLGLED---YFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDS-PRDIEAAKNAGIK 174


                  ....
gi 1721675436 224 TILV 227
Cdd:pfam13419 175 VIAV 178
PRK09449 PRK09449
dUMP phosphatase; Provisional
 181-259 1.13e-03

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 39.11  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 181 IGKPSPVMMRSAAAYMGLQP-EQVTIIGDTMETDIIGGIYMGFKTILVLSGIADKEQLIKygyrPHLVVDSVDEIEFPLK 259
Cdd:PRK09449  148 VAKPDVAIFDYALEQMGNPDrSRVLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIA----PTYQVSSLSELEQLLC 223
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 144-227 1.42e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 37.38  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 144 FIATNRDPSPRREGWNNLGIAATaamIEEATGREPFVIGKPSPVMMRSAAAYMGLQPEQVTIIGDTmETDIIGGIYMGFK 223
Cdd:cd01427    27 AIVTNRSREALRALLEKLGLGDL---FDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-ENDIEAARAAGGR 102


                  ....
gi 1721675436 224 TILV 227
Cdd:cd01427   103 TVAV 106
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
183-230 1.76e-03

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 38.26  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1721675436 183 KPSPVMMRSAAAYMGLQPEQVTIIGDTMEtDIIGGIYMGFKTILVLSG 230
Cdd:PRK08942  103 KPKPGMLLSIAERLNIDLAGSPMVGDSLR-DLQAAAAAGVTPVLVRTG 149
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 166-254 4.73e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 37.32  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 166 TAAMIEEATGREPF---VIG-------KPSPVMMRSAAAYMGLQPEQVTIIGDTMEtDIIGGIYMGFKTILVLSGIADKE 235
Cdd:PRK13288  111 TVEMGLKLTGLDEFfdvVITlddvehaKPDPEPVLKALELLGAKPEEALMVGDNHH-DILAGKNAGTKTAGVAWTIKGRE 189

                          90
                  ....*....|....*....
gi 1721675436 236 QLIKygYRPHLVVDSVDEI 254
Cdd:PRK13288  190 YLEQ--YKPDFMLDKMSDL 206
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 172-254 6.86e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 36.61  E-value: 6.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721675436 172 EATGREPFVI---------GKPSPVMMRSAAAYMGLQPEQVTIIGDTMEtDIIGGIYMGFKTILVLSGIADKEQLIKYGy 242
Cdd:cd07533   119 EQHGLGGYFDatrtaddtpSKPHPEMLREILAELGVDPSRAVMVGDTAY-DMQMAANAGAHAVGVAWGYHSLEDLRSAG- 196

                          90
                  ....*....|..
gi 1721675436 243 rPHLVVDSVDEI 254
Cdd:cd07533   197 -ADAVVDHFSEL 207
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 183-229 7.27e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 35.84  E-value: 7.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1721675436 183 KPSPVMMRSAAAYM-GLQPEQVTIIGDTMETDIIGGIYMGFKTILVLS 229
Cdd:TIGR01662  88 KPKPGMFLEALKRFnEIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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